An acyl-CoA thioesterase is essential for the biosynthesis of a key dauer pheromone in C. elegans.
Cell Chem Biol
; 31(5): 1011-1022.e6, 2024 May 16.
Article
em En
| MEDLINE
| ID: mdl-38183989
ABSTRACT
Methyl ketone (MK)-ascarosides represent essential components of several pheromones in Caenorhabditis elegans, including the dauer pheromone, which triggers the stress-resistant dauer larval stage, and the male-attracting sex pheromone. Here, we identify an acyl-CoA thioesterase, ACOT-15, that is required for the biosynthesis of MK-ascarosides. We propose a model in which ACOT-15 hydrolyzes the ß-keto acyl-CoA side chain of an ascaroside intermediate during ß-oxidation, leading to decarboxylation and formation of the MK. Using comparative metabolomics, we identify additional ACOT-15-dependent metabolites, including an unusual piperidyl-modified ascaroside, reminiscent of the alkaloid pelletierine. The ß-keto acid generated by ACOT-15 likely couples to 1-piperideine to produce the piperidyl ascaroside, which is much less dauer-inducing than the dauer pheromone, asc-C6-MK (ascr#2, 1). The bacterial food provided influences production of the piperidyl ascaroside by the worm. Our work shows how the biosynthesis of MK- and piperidyl ascarosides intersect and how bacterial food may impact chemical signaling in the worm.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Feromônios
/
Caenorhabditis elegans
Limite:
Animals
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article